scPDB - 4bhw entry

Protein Data Bank Entry:

PDB ID : 4bhw

Resolution :2.800 Å

Experimental Method : X-ray

Deposition Date : 2013-04-08

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	7.720	7.720	7.720	0.000	7.720	1

List of CHEMBLId :

CHEMBL505121

Binding Site :

Uniprot Annotation

Name:	Histone acetyltransferase p300
ID:	EP300_HUMAN
AC:	Q09472
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	96 %
B	4 %

Ligand binding site composition:

B-Factor:	50.961
Number of residues:	45
Including
Standard Amino Acids:	45
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.936	789.750

% Hydrophobic	% Polar
48.72	51.28
According to VolSite

Ligand :

HET Code:	01K
Formula:	C31H49N10O19P3S
Molecular weight:	990.763 g/mol
DrugBank ID:	-
Buried Surface Area:	54.24 %
Polar Surface area:	513.9 Å2

Number of
H-Bond Acceptors:	24
H-Bond Donors:	8
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	28

Mass center Coordinates

X	Y	Z
-33.2681	-23.0956	45.8391

Binding mode :

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Image generated by PoseView

Protein

Binding Site

Ligand

Interaction pattern

hydrophobic (CA)

aromatic (CZ)

hydrogen bond acceptor (O)

hydrogen bond acceptor/donor (OG)

hydrogen bond donor (N)

positively ionized (NZ)

negatively ionized (OD1)

metal (ZN)

Legend:

Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand

Image generated using PoseView by BioSolveIT

Ligand	Protein		Interaction
Atom	Atom	Residue	Distance (Å)	Angle (°)	Type
CG	CE1	TYR- 1397	3.81	0	Hydrophobic	false
O	OH	TYR- 1397	2.7	158.12	H-Bond (Protein Donor)	false
C8	CD1	LEU- 1398	4.34	0	Hydrophobic	false
C9	CD1	LEU- 1398	3.81	0	Hydrophobic	false
C21	CG	LEU- 1398	4.31	0	Hydrophobic	false
N17	O	LEU- 1398	2.9	167.23	H-Bond (Ligand Donor)	false
O32	N	LEU- 1398	3.08	141.35	H-Bond (Protein Donor)	false
C15	CB	ASP- 1399	4.46	0	Hydrophobic	false
C9	CB	SER- 1400	4.22	0	Hydrophobic	false
O45	NZ	LYS- 1407	3.23	149.55	H-Bond (Protein Donor)	false
O44	NZ	LYS- 1407	3.49	142.94	H-Bond (Protein Donor)	false
O45	NZ	LYS- 1407	3.23	0	Ionic (Protein Cationic)	false
O44	NZ	LYS- 1407	3.49	0	Ionic (Protein Cationic)	false
O44	NZ	LYS- 1407	3.65	0	Ionic (Protein Cationic)	false
O35	NH2	ARG- 1410	3.07	141.87	H-Bond (Protein Donor)	false
O35	NE	ARG- 1410	2.93	153.19	H-Bond (Protein Donor)	false
O46	NH2	ARG- 1410	3	141.99	H-Bond (Protein Donor)	false
O35	CZ	ARG- 1410	3.42	0	Ionic (Protein Cationic)	false
O36	OG1	THR- 1411	3	169.48	H-Bond (Protein Donor)	false
C6	CD2	TYR- 1414	4.22	0	Hydrophobic	false
C9	CD2	TYR- 1414	4.03	0	Hydrophobic	false
C21	CG2	ILE- 1435	4.19	0	Hydrophobic	false
NZ	O	TRP- 1436	2.78	156.95	H-Bond (Ligand Donor)	false
CB	CZ3	TRP- 1436	3.26	0	Hydrophobic	false
C63	CH2	TRP- 1436	4.08	0	Hydrophobic	false
CD	CE3	TRP- 1436	3.71	0	Hydrophobic	false
CD	CB	CYS- 1438	4.42	0	Hydrophobic	false
C15	CG	PRO- 1440	4.23	0	Hydrophobic	false
C15	CD2	TYR- 1446	4.1	0	Hydrophobic	false
C19	CE2	TYR- 1446	3.73	0	Hydrophobic	false
CG	CZ	TYR- 1446	3.81	0	Hydrophobic	false
C47	CB	LYS- 1456	4.33	0	Hydrophobic	false
N59	O	ILE- 1457	2.69	144.93	H-Bond (Ligand Donor)	false
DuAr	CZ	ARG- 1462	3.95	27.96	Pi/Cation	false
C8	CD1	LEU- 1463	4.07	0	Hydrophobic	false
S20	CD2	LEU- 1463	3.98	0	Hydrophobic	false
C6	CE2	TRP- 1466	3.55	0	Hydrophobic	false
C9	CZ2	TRP- 1466	4.25	0	Hydrophobic	false
O36	NE1	TRP- 1466	2.78	143.66	H-Bond (Protein Donor)	false
S20	CE2	PHE- 1467	3.45	0	Hydrophobic	false
C21	CZ	PHE- 1467	3.93	0	Hydrophobic	false